The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae
Autor(a) principal: | |
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Data de Publicação: | 2003 |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000400009 |
Resumo: | NADP+-dependent glutamate dehydrogenase (NADP+-Gdh) is the first step in ammonia assimilation pathway in Saccharomyces cerevisiae and the knowledge of its regulation is the key for many biotechnological purposes such as single cell protein production. The regulation of NADP+-Gdh activity in Kluyveromyces marxianus cells was evaluated under different ammonia supply in batch cultivations. The results showed that K. marxianus NADP+-Gdh activity is induced over a narrow range of extracellular ammonia supply, being repressed by both high ammonia concentration and the glutamate formed. This activity is not growth-associated and may function mainly to trace low amounts of ammonia after growth cessation. The results demonstrated that NADP+-Gdh may not be the main enzyme for ammonia assimilation in K. marxianus, as it has been postulated for K. lactis, instead is subjected to the same regulatory mechanism described for S. cerevisiae. |
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Brazilian Journal of Microbiology |
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spelling |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiaeammonia assimilationenzyme activityglutamate dehydrogenaseKluyveromyces marxianusNADP+-dependent glutamate dehydrogenase (NADP+-Gdh) is the first step in ammonia assimilation pathway in Saccharomyces cerevisiae and the knowledge of its regulation is the key for many biotechnological purposes such as single cell protein production. The regulation of NADP+-Gdh activity in Kluyveromyces marxianus cells was evaluated under different ammonia supply in batch cultivations. The results showed that K. marxianus NADP+-Gdh activity is induced over a narrow range of extracellular ammonia supply, being repressed by both high ammonia concentration and the glutamate formed. This activity is not growth-associated and may function mainly to trace low amounts of ammonia after growth cessation. The results demonstrated that NADP+-Gdh may not be the main enzyme for ammonia assimilation in K. marxianus, as it has been postulated for K. lactis, instead is subjected to the same regulatory mechanism described for S. cerevisiae.Sociedade Brasileira de Microbiologia2003-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000400009Brazilian Journal of Microbiology v.34 n.4 2003reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822003000400009info:eu-repo/semantics/openAccessMorais-Júnior,Marcos Antonio deeng2004-08-13T00:00:00Zoai:scielo:S1517-83822003000400009Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2004-08-13T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
title |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
spellingShingle |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae Morais-Júnior,Marcos Antonio de ammonia assimilation enzyme activity glutamate dehydrogenase Kluyveromyces marxianus |
title_short |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
title_full |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
title_fullStr |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
title_full_unstemmed |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
title_sort |
The NADP+-dependent glutamate dehydrogenase of the yeast Kluyveromyces marxianus responds to nitrogen repression similarly to Saccharomyces cerevisiae |
author |
Morais-Júnior,Marcos Antonio de |
author_facet |
Morais-Júnior,Marcos Antonio de |
author_role |
author |
dc.contributor.author.fl_str_mv |
Morais-Júnior,Marcos Antonio de |
dc.subject.por.fl_str_mv |
ammonia assimilation enzyme activity glutamate dehydrogenase Kluyveromyces marxianus |
topic |
ammonia assimilation enzyme activity glutamate dehydrogenase Kluyveromyces marxianus |
description |
NADP+-dependent glutamate dehydrogenase (NADP+-Gdh) is the first step in ammonia assimilation pathway in Saccharomyces cerevisiae and the knowledge of its regulation is the key for many biotechnological purposes such as single cell protein production. The regulation of NADP+-Gdh activity in Kluyveromyces marxianus cells was evaluated under different ammonia supply in batch cultivations. The results showed that K. marxianus NADP+-Gdh activity is induced over a narrow range of extracellular ammonia supply, being repressed by both high ammonia concentration and the glutamate formed. This activity is not growth-associated and may function mainly to trace low amounts of ammonia after growth cessation. The results demonstrated that NADP+-Gdh may not be the main enzyme for ammonia assimilation in K. marxianus, as it has been postulated for K. lactis, instead is subjected to the same regulatory mechanism described for S. cerevisiae. |
publishDate |
2003 |
dc.date.none.fl_str_mv |
2003-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000400009 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822003000400009 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1517-83822003000400009 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.34 n.4 2003 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122199714562048 |